{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T19:34:51Z","timestamp":1790537691608,"version":"4.1.0"},"reference-count":70,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,7,13]],"date-time":"2024-07-13T00:00:00Z","timestamp":1720828800000},"content-version":"am","delay-in-days":347,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["NINDS-R01NS128358"],"award-info":[{"award-number":["NINDS-R01NS128358"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["bmn.com","cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Trends in Biochemical Sciences"],"published-print":{"date-parts":[[2023,8]]},"DOI":"10.1016\/j.tibs.2023.04.003","type":"journal-article","created":{"date-parts":[[2023,5,6]],"date-time":"2023-05-06T16:11:24Z","timestamp":1683389484000},"page":"689-698","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"title":["Tudor\u2013dimethylarginine interactions: the condensed version"],"prefix":"10.1016","volume":"48","author":[{"given":"Daniela","family":"\u0160im\u010d\u00edkov\u00e1","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara","family":"Gelles-Watnick","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3835-6761","authenticated-orcid":false,"given":"Karla M.","family":"Neugebauer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.tibs.2023.04.003_bb0005","doi-asserted-by":"crossref","first-page":"2462","DOI":"10.1021\/acs.biochem.7b01262","article-title":"Dynamics and function of nuclear bodies during embryogenesis","volume":"57","author":"Arias Escayola","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.tibs.2023.04.003_bb0010","doi-asserted-by":"crossref","first-page":"eaaf4382","DOI":"10.1126\/science.aaf4382","article-title":"Liquid phase condensation in cell physiology and disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.tibs.2023.04.003_bb0015","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular condensates: organizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.tibs.2023.04.003_bb0020","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a034926","article-title":"The RNA base-pairing problem and base-pairing solutions","volume":"10","author":"Lu","year":"2018","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.tibs.2023.04.003_bb0025","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1016\/j.molcel.2020.08.004","article-title":"Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change","volume":"79","author":"Jalihal","year":"2020","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0030","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1038\/s41467-021-21181-9","article-title":"Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions","volume":"12","author":"Krainer","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2023.04.003_bb0035","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1016\/j.molcel.2018.02.004","article-title":"Ubiquitin modulates liquid-liquid phase separation of UBQLN2 via disruption of multivalent interactions","volume":"69","author":"Dao","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0040","doi-asserted-by":"crossref","first-page":"eaay7108","DOI":"10.1126\/science.aay7108","article-title":"Endoplasmic reticulum contact sites regulate the dynamics of membraneless organelles","volume":"367","author":"Lee","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.tibs.2023.04.003_bb0045","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1038\/s41586-018-0279-8","article-title":"Kinase-controlled phase transition of membraneless organelles in mitosis","volume":"559","author":"Rai","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.tibs.2023.04.003_bb0050","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1016\/j.molcel.2021.01.016","article-title":"Stress-induced nuclear condensation of NELF drives transcriptional downregulation","volume":"81","author":"Rawat","year":"2021","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0055","doi-asserted-by":"crossref","first-page":"1360","DOI":"10.3390\/ijms19051360","article-title":"Acetylation disfavors tau phase separation","volume":"19","author":"Ferreon","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.tibs.2023.04.003_bb0060","doi-asserted-by":"crossref","first-page":"2226","DOI":"10.1128\/MCB.01102-15","article-title":"The C-terminal RGG domain of human Lsm4 promotes processing body formation stimulated by arginine dimethylation","volume":"36","author":"Arribas-Layton","year":"2016","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.tibs.2023.04.003_bb0065","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1016\/j.molcel.2015.01.013","article-title":"Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles","volume":"57","author":"Nott","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0070","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/j.molcel.2017.12.022","article-title":"Mechanistic view of hnRNPA2 low-complexity domain structure, interactions, and phase separation altered by mutation and arginine methylation","volume":"69","author":"Ryan","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0075","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.1038\/nsmb.2185","article-title":"Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins","volume":"18","author":"Tripsianes","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.tibs.2023.04.003_bb0080","doi-asserted-by":"crossref","first-page":"3612","DOI":"10.1016\/j.cell.2021.05.008","article-title":"DMA\u2013tudor interaction modules control the specificity of in vivo condensates","volume":"184","author":"Courchaine","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0085","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/j.celrep.2014.12.030","article-title":"SART3-dependent accumulation of incomplete spliceosomal snRNPs in Cajal bodies","volume":"10","author":"Novotny","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.tibs.2023.04.003_bb0090","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/0092-8674(95)90460-3","article-title":"Identification and characterization of a spinal muscular atrophy-determining gene","volume":"80","author":"Lefebvre","year":"1995","journal-title":"Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0095","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1038\/cr.2014.63","article-title":"Structure and domain organization of Drosophila Tudor","volume":"24","author":"Ren","year":"2014","journal-title":"Cell Res."},{"key":"10.1016\/j.tibs.2023.04.003_bb0100","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1010249","article-title":"TDRD3 is an antiviral restriction factor that promotes IFN signaling with G3BP1","volume":"18","author":"Deater","year":"2022","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.tibs.2023.04.003_bb0105","doi-asserted-by":"crossref","first-page":"16048","DOI":"10.1038\/celldisc.2016.48","article-title":"Arginine methylation of USP9X promotes its interaction with TDRD3 and its anti-apoptotic activities in breast cancer cells","volume":"3","author":"Narayanan","year":"2017","journal-title":"Cell Discov."},{"key":"10.1016\/j.tibs.2023.04.003_bb0110","doi-asserted-by":"crossref","first-page":"3061","DOI":"10.1093\/nar\/gky103","article-title":"Arginine methylation of the C-terminus RGG motif promotes TOP3B topoisomerase activity and stress granule localization","volume":"46","author":"Huang","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.tibs.2023.04.003_bb0115","first-page":"61","article-title":"The Tudor domain protein Tapas, a homolog of the vertebrate Tdrd7, functions in the piRNA pathway to regulate retrotransposons in germline of Drosophila melanogaster","volume":"12","author":"Patil","year":"2014","journal-title":"BMC Biol."},{"key":"10.1016\/j.tibs.2023.04.003_bb0120","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2020.108597","article-title":"Deciphering piRNA biogenesis through cytoplasmic granules, mitochondria and exosomes","volume":"695","author":"Pippadpally","year":"2020","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.tibs.2023.04.003_bb0125","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2022.818302","article-title":"The Tudor domain-containing protein, Kotsubu (CG9925), localizes to the nuage and functions in piRNA biogenesis in D. melanogaster","volume":"9","author":"Lim","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.tibs.2023.04.003_bb0130","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.devcel.2018.07.009","article-title":"Tdrd6a regulates the aggregation of Buc into functional subcellular compartments that drive germ cell specification","volume":"46","author":"Roovers","year":"2018","journal-title":"Dev. Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0135","doi-asserted-by":"crossref","DOI":"10.15252\/embr.201947708","article-title":"Requirements for multivalent Yb body assembly in transposon silencing in Drosophila","volume":"20","author":"Hirakata","year":"2019","journal-title":"EMBO Rep."},{"key":"10.1016\/j.tibs.2023.04.003_bb0140","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1016\/j.str.2021.06.007","article-title":"Inherent backbone dynamics fine-tune the functional plasticity of Tudor domains","volume":"29","author":"Kawale","year":"2021","journal-title":"Structure"},{"key":"10.1016\/j.tibs.2023.04.003_bb0145","doi-asserted-by":"crossref","first-page":"1925","DOI":"10.15252\/embj.201490350","article-title":"Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization","volume":"34","author":"Neuenkirchen","year":"2015","journal-title":"EMBO J."},{"key":"10.1016\/j.tibs.2023.04.003_bb0150","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1007\/s00412-017-0637-6","article-title":"UsnRNP biogenesis: mechanisms and regulation","volume":"126","author":"Gruss","year":"2017","journal-title":"Chromosoma"},{"key":"10.1016\/j.tibs.2023.04.003_bb0155","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1038\/s41467-021-21529-1","article-title":"Interaction of 7SK with the Smn complex modulates snRNP production","volume":"12","author":"Ji","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2023.04.003_bb0160","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1146\/annurev-genom-102319-103602","article-title":"Twenty-five years of spinal muscular atrophy research: from phenotype to genotype to therapy, and what comes next","volume":"21","author":"Wirth","year":"2020","journal-title":"Annu. Rev. Genomics Hum. Genet."},{"key":"10.1016\/j.tibs.2023.04.003_bb0165","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1038\/nature16469","article-title":"SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination","volume":"529","author":"Zhao","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.tibs.2023.04.003_bb0170","doi-asserted-by":"crossref","first-page":"5453","DOI":"10.1038\/s41467-022-33229-5","article-title":"A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP II","volume":"13","author":"Liu","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2023.04.003_bb0175","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.febslet.2004.07.010","article-title":"Survival motor neuron protein facilitates assembly of stress granules","volume":"572","author":"Hua","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1016\/j.tibs.2023.04.003_bb0180","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1038\/s41556-020-00577-7","article-title":"SMN-primed ribosomes modulate the translation of transcripts related to spinal muscular atrophy","volume":"22","author":"Lauria","year":"2020","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.tibs.2023.04.003_bb0185","doi-asserted-by":"crossref","first-page":"11559","DOI":"10.1523\/JNEUROSCI.1528-17.2017","article-title":"HuD and the survival motor neuron protein interact in motoneurons and are essential for motoneuron development, function, and mRNA regulation","volume":"37","author":"Hao le","year":"2017","journal-title":"J. Neurosci."},{"key":"10.1016\/j.tibs.2023.04.003_bb0190","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1016\/j.celrep.2017.01.059","article-title":"The survival of motor neuron protein acts as a molecular chaperone for mRNP assembly","volume":"18","author":"Donlin-Asp","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.tibs.2023.04.003_bb0195","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2021.639904","article-title":"Fluorescence correlation spectroscopy reveals survival motor neuron oligomerization but no active transport in motor axons of a zebrafish model for spinal muscular atrophy","volume":"9","author":"Koh","year":"2021","journal-title":"Front. Cell Develop. Biol."},{"key":"10.1016\/j.tibs.2023.04.003_bb0200","first-page":"804","article-title":"SMN affects membrane remodelling and anchoring of the protein synthesis machinery","volume":"129","author":"Gabanella","year":"2016","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.tibs.2023.04.003_bb0205","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/j.celrep.2017.10.010","article-title":"In vivo translatome profiling in spinal muscular atrophy reveals a role for SMN protein in ribosome biology","volume":"21","author":"Bernabo","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.tibs.2023.04.003_bb0210","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1016\/j.scib.2021.01.004","article-title":"A systematic survey of PRMT interactomes reveals the key roles of arginine methylation in the global control of RNA splicing and translation","volume":"66","author":"Wei","year":"2021","journal-title":"Sci. Bull."},{"key":"10.1016\/j.tibs.2023.04.003_bb0215","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1016\/j.celrep.2018.09.084","article-title":"Active ribosome profiling with RiboLace","volume":"25","author":"Clamer","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.tibs.2023.04.003_bb0220","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1038\/s41580-019-0155-x","article-title":"The regulation, functions and clinical relevance of arginine methylation","volume":"20","author":"Guccione","year":"2019","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.tibs.2023.04.003_bb0225","doi-asserted-by":"crossref","first-page":"1473","DOI":"10.1016\/j.celrep.2018.01.031","article-title":"Citrullination of RGG motifs in FET proteins by PAD4 regulates protein aggregation and ALS susceptibility","volume":"22","author":"Tanikawa","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.tibs.2023.04.003_bb0230","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1126\/science.1175865","article-title":"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing","volume":"325","author":"Webby","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.tibs.2023.04.003_bb0235","doi-asserted-by":"crossref","first-page":"32","DOI":"10.3389\/fgene.2017.00032","article-title":"Jmjd6, a JmjC dioxygenase with many interaction partners and pleiotropic functions","volume":"8","author":"Kwok","year":"2017","journal-title":"Front. Genet."},{"key":"10.1016\/j.tibs.2023.04.003_bb0240","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2201483119","article-title":"Widespread hydroxylation of unstructured lysine-rich protein domains by JMJD6","volume":"119","author":"Cockman","year":"2022","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tibs.2023.04.003_bb0245","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2200753119","article-title":"A specific JMJD6 inhibitor potently suppresses multiple types of cancers both in vitro and in vivo","volume":"119","author":"Xiao","year":"2022","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tibs.2023.04.003_bb0250","doi-asserted-by":"crossref","first-page":"3123","DOI":"10.1021\/acs.jproteome.0c00116","article-title":"Improved discrimination of asymmetric and symmetric arginine dimethylation by optimization of the normalized collision energy in liquid chromatography-mass spectrometry proteomics","volume":"19","author":"Hartel","year":"2020","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.tibs.2023.04.003_bb0255","doi-asserted-by":"crossref","first-page":"2149","DOI":"10.1074\/mcp.RA119.001625","article-title":"Deep protein methylation profiling by combined chemical and immunoaffinity approaches reveals novel PRMT1 targets","volume":"18","author":"Hartel","year":"2019","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.tibs.2023.04.003_bb0260","doi-asserted-by":"crossref","first-page":"1574","DOI":"10.1021\/acs.jproteome.9b00633","article-title":"Middle-down proteomics reveals dense sites of methylation and phosphorylation in arginine-rich RNA-binding proteins","volume":"19","author":"Kundinger","year":"2020","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.tibs.2023.04.003_bb0265","doi-asserted-by":"crossref","first-page":"17454","DOI":"10.1074\/jbc.RA118.004028","article-title":"CARM1-mediated methylation of protein arginine methyltransferase 5 represses human gamma-globin gene expression in erythroleukemia cells","volume":"293","author":"Nie","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2023.04.003_bb0270","doi-asserted-by":"crossref","first-page":"4357","DOI":"10.1016\/j.molcel.2021.09.011","article-title":"Cellular pathways influenced by protein arginine methylation: Implications for cancer","volume":"81","author":"Xu","year":"2021","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0275","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.72867","article-title":"Type I and II PRMTs inversely regulate post-transcriptional intron detention through Sm and CHTOP methylation","volume":"11","author":"Maron","year":"2022","journal-title":"Elife"},{"key":"10.1016\/j.tibs.2023.04.003_bb0280","doi-asserted-by":"crossref","first-page":"1944","DOI":"10.1074\/jbc.RA118.004928","article-title":"The 40S ribosomal protein uS5 (RPS2) assembles into an extraribosomal complex with human ZNF277 that competes with the PRMT3-uS5 interaction","volume":"294","author":"Dionne","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2023.04.003_bb0285","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1016\/j.cell.2018.03.056","article-title":"FUS phase separation is modulated by a molecular chaperone and methylation of arginine cation-pi interactions","volume":"173","author":"Qamar","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0290","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1016\/j.cell.2018.03.004","article-title":"Phase separation of FUS is suppressed by its nuclear import receptor and arginine methylation","volume":"173","author":"Hofweber","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0295","doi-asserted-by":"crossref","first-page":"22671","DOI":"10.1074\/jbc.M116.739573","article-title":"Arginine demethylation of G3BP1 promotes stress granule assembly","volume":"291","author":"Tsai","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2023.04.003_bb0300","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/s41418-019-0350-5","article-title":"UBAP2L arginine methylation by PRMT1 modulates stress granule assembly","volume":"27","author":"Huang","year":"2020","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.tibs.2023.04.003_bb0305","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1038\/srep01311","article-title":"Loss of the major Type I arginine methyltransferase PRMT1 causes substrate scavenging by other PRMTs","volume":"3","author":"Dhar","year":"2013","journal-title":"Sci. Rep."},{"key":"10.1016\/j.tibs.2023.04.003_bb0310","doi-asserted-by":"crossref","first-page":"102971","DOI":"10.1016\/j.isci.2021.102971","article-title":"Independent transcriptomic and proteomic regulation by type I and II protein arginine methyltransferases","volume":"24","author":"Maron","year":"2021","journal-title":"iScience"},{"key":"10.1016\/j.tibs.2023.04.003_bb0315","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1126\/science.252.5009.1167","article-title":"Arginine-mediated RNA recognition: the arginine fork","volume":"252","author":"Calnan","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.tibs.2023.04.003_bb0320","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0325","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1016\/j.cell.2006.10.043","article-title":"Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair","volume":"127","author":"Botuyan","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.tibs.2023.04.003_bb0330","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1038\/sj.embor.7400625","article-title":"Tudor, MBT and chromo domains gauge the degree of lysine methylation","volume":"7","author":"Kim","year":"2006","journal-title":"EMBO Rep."},{"key":"10.1016\/j.tibs.2023.04.003_bb0335","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1038\/s41467-022-28019-y","article-title":"53BP1 regulates heterochromatin through liquid phase separation","volume":"13","author":"Zhang","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2023.04.003_bb0340","doi-asserted-by":"crossref","first-page":"11748","DOI":"10.1093\/nar\/gks929","article-title":"Recognition of asymmetrically dimethylated arginine by TDRD3","volume":"40","author":"Sikorsky","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.tibs.2023.04.003_bb0345","doi-asserted-by":"crossref","first-page":"18398","DOI":"10.1073\/pnas.1013106107","article-title":"Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain","volume":"107","author":"Liu","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tibs.2023.04.003_bb0350","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1016\/j.str.2004.06.014","article-title":"The Tudor tandem of 53BP1: a new structural motif involved in DNA and RG-rich peptide binding","volume":"12","author":"Charier","year":"2004","journal-title":"Structure"}],"container-title":["Trends in Biochemical Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968000423000877?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968000423000877?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T21:48:03Z","timestamp":1760824083000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968000423000877"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,8]]},"references-count":70,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2023,8]]}},"alternative-id":["S0968000423000877"],"URL":"https:\/\/doi.org\/10.1016\/j.tibs.2023.04.003","relation":{},"ISSN":["0968-0004"],"issn-type":[{"value":"0968-0004","type":"print"}],"subject":[],"published":{"date-parts":[[2023,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Tudor\u2013dimethylarginine interactions: the condensed version","name":"articletitle","label":"Article Title"},{"value":"Trends in Biochemical Sciences","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.tibs.2023.04.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}